ReviewJournal of neural transmission (Vienna, Austria : 1996)2014
Complex molecular regulation of tyrosine hydroxylase.
Review in Journal of neural transmission (Vienna, Austria : 1996), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
55 citing papers in PubMed, 124 citations in OpenAlex.
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- Theranekron attenuates lipopolysaccharide-induced neuroinflammation via NLRP3 inflammasome modulation.Molecular biology reports · 2026Article
- Agonism of FFA4/GPR120 activates tyrosine hydroxylase and confers neuroprotection from 6-OHDA-induced cytotoxicity in PC12 cells and in a rat 6-OHDA model of Parkinson's disease.Biochemical pharmacology · 2026Article
- Slow-Timescale Regulation of Dopamine Release and Mating Drive Over Days.bioRxiv : the preprint server for biology · 2025Article
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- Dietary Iron Intake and Mental and Behavioral Disorders Due to Use of Tobacco: A UK Biobank Study.Nutrients · 2024Article
- Hyperphenylalaninemia and serotonin deficiency in Dnajc12-deficient mice.Communications biology · 2024Article
- Cluster Headache and Hypoxia: Breathing New Life into an Old Theory, with Novel Implications.Neurology international · 2024Review
- Phosphodiesterase inhibition and Gucy2C activation enhance tyrosine hydroxylase Ser40 phosphorylation and improve 6-hydroxydopamine-induced motor deficits.Cell & bioscience · 2024Article
- Dopamine synthesis and transport: current and novel therapeutics for parkinsonisms.Biochemical Society transactions · 2024Review
- N-Acetylcysteine Treatment May Compensate Motor Impairments through Dopaminergic Transmission Modulation in a Striatal 6-Hydroxydopamine Parkinson's Disease Rat Model.Antioxidants (Basel, Switzerland) · 2023Article
- Association ofFrontiers in psychiatry · 2023Article
- The neuromodulatory effects of flavonoids and gut Microbiota through the gut-brain axis.Frontiers in cellular and infection microbiology · 2023Review
- Roles of Pancreatic Islet Catecholamine Neurotransmitters in Glycemic Control and in Antipsychotic Drug-Induced Dysglycemia.Diabetes · 2023Review
- Locus coeruleus catecholamines link neuroticism and vulnerability to tau pathology in aging.NeuroImage · 2022Article
- Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation.Nature communications · 2022Article
- Zinc antagonizes iron-regulation of tyrosine hydroxylase activity and dopamine production in Drosophila melanogaster.BMC biology · 2021Article
- The essential role of transcription factor Pitx3 in preventing mesodiencephalic dopaminergic neurodegeneration and maintaining neuronal subtype identities during aging.Cell death & disease · 2021Article
- cAMP Response Element Binding-Protein- and Phosphorylation-Dependent Regulation of Tyrosine Hydroxylase by PAK4: Implications for Dopamine Replacement Therapy.Molecules and cells · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Tyrosine hydroxylase, the rate-limiting enzyme in catecholamine biosynthesis, is strictly controlled by several interrelated regulatory mechanisms. Enzyme synthesis is controlled by epigenetic factors, transcription factors, and mRNA levels. Enzyme activity is regulated by end-product feedback inhibition. Phosphorylation of the enzyme is catalyzed by several protein kinases and dephosphorylation is mediated by two protein phosphatases that establish a sensitive process for regulating enzyme activity on a minute-to-minute basis. Interactions between tyrosine hydroxylase and other proteins introduce additional layers to the already tightly controlled production of catecholamines. Tyrosine hydroxylase degradation by the ubiquitin-proteasome coupled pathway represents yet another mechanism of regulation. Here, we revisit the myriad mechanisms that regulate tyrosine hydroxylase expression and activity and highlight their physiological importance in the control of catecholamine biosynthesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.